Note on the evolutionary insights of CDPKs and CRKs through intron/exon analysis, proposing a monophyletic origin and highlighting the role of ancient intron-mediated gene fusion in the origin of CDPKs.
Note on the evolutionary insights of CDPKs and CRKs through intron/exon analysis, proposing a monophyletic origin and highlighting the role of ancient intron-mediated gene fusion in the origin of CDPKs.
Overview of the plant-specific CDPK-SnRK superfamily, including CDPKs, CRKs, CCaMKs, SnRKs, and their Ca²⁺ regulatory mechanisms. Models of activation and functional diversity of Ca²⁺ decoding mechanisms are discussed.
Overview of the plant-specific CDPK-SnRK superfamily, including CDPKs, CRKs, CCaMKs, SnRKs, and their Ca²⁺ regulatory mechanisms. Models of activation and functional diversity of Ca²⁺ decoding mechanisms are discussed.
Note on the differential calcium sensitivity among Arabidopsis CDPK isoforms, highlighting the diversity of activation mechanisms and implications for calcium signaling in plants.
Note on the differential calcium sensitivity among Arabidopsis CDPK isoforms, highlighting the diversity of activation mechanisms and implications for calcium signaling in plants.
A fascinating study revealing that TgCDPK1 is stabilized and activated via an allosteric mechanism involving its regulatory CAD domain, challenging classical models of calcium-dependent kinase activation.
A fascinating study revealing that TgCDPK1 is stabilized and activated via an allosteric mechanism involving its regulatory CAD domain, challenging classical models of calcium-dependent kinase activation.
A landmark structural study revealing how apicomplexan CDPKs (TgCDPK1/3, CpCDPK) undergo dramatic conformational changes upon calcium binding to shift from an autoinhibited to an active state.
A landmark structural study revealing how apicomplexan CDPKs (TgCDPK1/3, CpCDPK) undergo dramatic conformational changes upon calcium binding to shift from an autoinhibited to an active state.
Notes on a 2017 Scientific Reports study proposing the Calmodulin-Fused Kinase (CFK) family as the principal system for converting calcium signals to protein phosphorylation responses in plants, based on deep phylogenetic analysis tracing their evolutionary origins and functional diversification.
Notes on a 2017 Scientific Reports study proposing the Calmodulin-Fused Kinase (CFK) family as the principal system for converting calcium signals to protein phosphorylation responses in plants, based on deep phylogenetic analysis tracing their evolutionary origins and functional diversification.
Note on the detailed structural study of CDPK activation, focusing on apicomplexan CAD conformations (CpCDPK, PfCDPK3), offering new insight into a potentially universal activation mechanism for CDPKs.
Note on the detailed structural study of CDPK activation, focusing on apicomplexan CAD conformations (CpCDPK, PfCDPK3), offering new insight into a potentially universal activation mechanism for CDPKs.
Note on the discovery that the variable N-terminal domain of CDPK1 controls substrate specificity—offering a new mechanism to engineer signaling specificity in plants.
